A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level information reveals key intermolecular contacts identifying new potentially druggable areas on cytochrome c and Bcl-x(L). Involvement of residues on cytochrome c other than those in its complexes with electron transfer partners is apparent. Key differences in the contact area also exist between the Bcl-x(L) adduct with the Bak peptide and that with cytochrome c. The present model provides insights to the mechanism by which cytochrome c translocated to cytosol can be intercepted, so that the apoptosome is not assembled.

The Anti-Apoptotic Bcl-xL Protein, a New Piece in the Puzzle of Cytochrome C Interactome / I.Bertini; S.Chevance; R.Del Conte; D.Lalli; P.Turano. - In: PLOS ONE. - ISSN 1932-6203. - ELETTRONICO. - 6(4):(2011), pp. e18329-e18329. [10.1371/journal.pone.0018329]

The Anti-Apoptotic Bcl-xL Protein, a New Piece in the Puzzle of Cytochrome C Interactome

BERTINI, IVANO;DEL CONTE, REBECCA;LALLI, DANIELA;TURANO, PAOLA
2011

Abstract

A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level information reveals key intermolecular contacts identifying new potentially druggable areas on cytochrome c and Bcl-x(L). Involvement of residues on cytochrome c other than those in its complexes with electron transfer partners is apparent. Key differences in the contact area also exist between the Bcl-x(L) adduct with the Bak peptide and that with cytochrome c. The present model provides insights to the mechanism by which cytochrome c translocated to cytosol can be intercepted, so that the apoptosome is not assembled.
2011
6(4)
e18329
e18329
I.Bertini; S.Chevance; R.Del Conte; D.Lalli; P.Turano
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/432364
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